Exploring liquid-liquid phase separation in the organisation of Golgi matrix proteins

• Published in: Biochimica et biophysica acta. Proteins and proteomics Vol. 1872; no. 5; p. 141029
• Main Authors: Mendes, Luis Felipe S., Oliveira, Carolina G., Simões, Kevin F., Kava, Emanuel, Costa-Filho, Antonio J.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2024
• Subjects: Animals; Biomolecular condensates; Golgi Apparatus - metabolism; Golgi complex; Golgi Matrix Proteins - metabolism; Golgins; GRASPs; Humans; Intrinsically disordered proteins; Phase Separation; Protein Transport; GRASPs; Golgi complex; Intrinsically disordered proteins; Biomolecular condensates; Golgins
• ISSN: 1570-9639; 1878-1454; 1878-1454
• DOI: 10.1016/j.bbapap.2024.141029

The Golgi apparatus is a critical organelle in protein sorting and lipid metabolism. Characterized by its stacked, flattened cisternal structure, the Golgi exhibits distinct polarity with its cis- and trans-faces orchestrating various protein maturation and transport processes. At the heart of its structural integrity and organisation are the Golgi Matrix Proteins (GMPs), predominantly comprising Golgins and GRASPs. These proteins contribute to this organelle's unique stacked and polarized structure and ensure the precise localization of Golgi-resident enzymes, which is crucial for accurate protein processing. Despite over a century of research since its discovery, the Golgi architecture's intricate mechanisms still need to be fully understood. Here, we discuss that GMPs across different Eukaryotic lineages present a significant tendency to form biomolecular condensates. Moreover, we validated experimentally that members of the GRASP family also exhibit a strong tendency. Our findings offer a new perspective on the possible roles of protein disorder and condensation of GMPs in the Golgi organisation. •Discovered widespread LLPS-propensity among Golgi Matrix Proteins across various eukaryotic lineages, suggesting a fundamental process in Golgi apparatus organisation.•Experimentally confirming LLPS-propensity in the GRASP family•Unveiled intrinsic disorder prevalence within GMPs, indicating a conserved structural feature that facilitates condensation and Golgi functionality across eukaryotes.•The proposed evolutionary significance of biomolecular condensation and intrinsic disorder in GMPs for maintaining Golgi apparatus structure offers new insights into cellular organisation principles.